Research workbench
Crystal structure of the DNMT3A add domain in complex with histone H3
Analyse Crystal structure of the DNMT3A add domain in complex with histone H3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A1B
- Type
- protein
- Length
- 148 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (cytosine-5)-methyltransferase 3A, histone H3.1
- EC
- 2.1.1.37
- UniProt
- P68431, Q9Y6K1
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA (cytosine-5)-methyltransferase 3A, histone H3.1 (EC 2.1.1.37) | protein | 148 | 32% helix, 16% strand | P68431, Q9Y6K1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.34 | 0.73 | 19 | EDO |
Compared structures
- 3A1B · Crystal structure of the DNMT3A ADD domain in complex with histone H3 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y6K1 · AlphaFold monomer V2.0 prediction for DNA (cytosine-5)-methyltransferase 3A (Q9Y6K1) · a predicted model of the same protein · chain A against A, TM-score 0.93
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P68431
- Every structure of UniProt Q9Y6K1
- Elsewhere: RCSB PDB 3A1B · PDBe 3A1B · UniProt P68431 · UniProt Q9Y6K1
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